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Volumn 158, Issue 7, 2002, Pages 1263-1275

T cell receptor ligation induces the formation of dynamically regulated signaling assemblies

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CELL PROTEIN; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; LAT PROTEIN; PHOSPHOTYROSINE; PROTEIN GADS; PROTEIN KINASE ZAP 70; PROTEIN SLP 67; PROTEIN TYROSINE KINASE; T LYMPHOCYTE RECEPTOR; UNCLASSIFIED DRUG;

EID: 0037144842     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200203043     Document Type: Article
Times cited : (526)

References (55)
  • 2
    • 0034005120 scopus 로고    scopus 로고
    • Cytoskeletal polarization and redistribution of cell-surface molecules during T cell antigen recognition
    • Anton van der Merwe, P., S.J. Davis, A.S. Shaw, and M.L. Dustin. 2000. Cytoskeletal polarization and redistribution of cell-surface molecules during T cell antigen recognition. Semin. Immunol. 12:5-21.
    • (2000) Semin. Immunol. , vol.12 , pp. 5-21
    • Anton van der Merwe, P.1    Davis, S.J.2    Shaw, A.S.3    Dustin, M.L.4
  • 3
    • 0035654908 scopus 로고    scopus 로고
    • Distinct patterns of membrane microdomain partitioning in Th1 and Th2 cells
    • Balamuth, F., D. Leitenberg, J. Unternaehrer, I. Mellman, and K. Bottomly. 2001. Distinct patterns of membrane microdomain partitioning in Th1 and Th2 cells. Immunity. 15:729-738.
    • (2001) Immunity , vol.15 , pp. 729-738
    • Balamuth, F.1    Leitenberg, D.2    Unternaehrer, J.3    Mellman, I.4    Bottomly, K.5
  • 5
    • 0342313755 scopus 로고    scopus 로고
    • Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation
    • Brdicka, T., D. Pavlistova, A. Leo, E. Bruyns, V. Korinek, P. Angelisova, J. Scherer, A. Shevchenko, I. Hilgert, J. Cerny, et al. 2000. Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation. J. Exp. Med. 191:1591-1604.
    • (2000) J. Exp. Med. , vol.191 , pp. 1591-1604
    • Brdicka, T.1    Pavlistova, D.2    Leo, A.3    Bruyns, E.4    Korinek, V.5    Angelisova, P.6    Scherer, J.7    Shevchenko, A.8    Hilgert, I.9    Cerny, J.10
  • 7
    • 0034695633 scopus 로고    scopus 로고
    • Biochemical interactions integrating Itk with the T cell teceptor-initiated signaling cascade
    • Bunnell, S.C., M. Diehn, M.B., Yaffe, P.R. Findell, L.C. Cantley, and L.J. Berg. 2000. Biochemical interactions integrating Itk with the T cell teceptor-initiated signaling cascade. J. Biol. Chem. 275:2219-2230.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2219-2230
    • Bunnell, S.C.1    Diehn, M.2    Yaffe, M.B.3    Findell, P.R.4    Cantley, L.C.5    Berg, L.J.6
  • 8
    • 0035075507 scopus 로고    scopus 로고
    • Dynamic actin polymerization drives T cell receptor-induced spreading: A role for the signal transduction adaptor LAT
    • Bunnell, S.C., V. Kapoor, R.P., Trible, W. Zhang, and L.E. Samelson. 2001. Dynamic actin polymerization drives T cell receptor-induced spreading: a role for the signal transduction adaptor LAT. Immunity. 14:315-329.
    • (2001) Immunity , vol.14 , pp. 315-329
    • Bunnell, S.C.1    Kapoor, V.2    Trible, R.P.3    Zhang, W.4    Samelson, L.E.5
  • 9
    • 0031975838 scopus 로고    scopus 로고
    • Essential role for G protein-coupled receptor endocytosis in the activation of mitogen-activated protein kinase
    • Daaka, Y., L.M. Luttrell, S. Ahn, G.J. Della Rocca, S.S. Ferguson, M.G. Caron, and R.J. Lefkowitz. 1998. Essential role for G protein-coupled receptor endocytosis in the activation of mitogen-activated protein kinase. J. Biol. Chem. 273: 685-688.
    • (1998) J. Biol. Chem. , vol.273 , pp. 685-688
    • Daaka, Y.1    Luttrell, L.M.2    Ahn, S.3    Della Rocca, G.J.4    Ferguson, S.S.5    Caron, M.G.6    Lefkowitz, R.J.7
  • 10
    • 0034649643 scopus 로고    scopus 로고
    • Information transfer at the immunologicalsynapse
    • Delon, J., and R.N. Germain. 2000. Information transfer at the immunologicalsynapse. Curr. Biol. 10:R923-R933.
    • (2000) Curr. Biol. , vol.10
    • Delon, J.1    Germain, R.N.2
  • 11
    • 0031936042 scopus 로고    scopus 로고
    • Imaging antigen recognition by naive CD4+ T cells: Compulsory cytoskeletal alterations for the triggering of an intracellular calcium response
    • Delon, J., N. Bercovici, R. Liblau, and A. Trautmann. 1998. Imaging antigen recognition by naive CD4+ T cells: compulsory cytoskeletal alterations for the triggering of an intracellular calcium response. Eur. J. Immunol. 28:716-729.
    • (1998) Eur. J. Immunol. , vol.28 , pp. 716-729
    • Delon, J.1    Bercovici, N.2    Liblau, R.3    Trautmann, A.4
  • 12
    • 0035652354 scopus 로고    scopus 로고
    • Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin
    • Delon, J., K. Kaibuchi, and R.N. Germain. 2001. Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin. Immunity. 15:691-701.
    • (2001) Immunity , vol.15 , pp. 691-701
    • Delon, J.1    Kaibuchi, K.2    Germain, R.N.3
  • 13
    • 0034232037 scopus 로고    scopus 로고
    • The immunological synapse and the actin cytoskeleton: Molecular hardware for T cell signaling
    • Dustin, M.L., and J.A. Cooper. 2000. The immunological synapse and the actin cytoskeleton: molecular hardware for T cell signaling. Nat. Immunol. 1:23-29.
    • (2000) Nat. Immunol. , vol.1 , pp. 23-29
    • Dustin, M.L.1    Cooper, J.A.2
  • 14
    • 0032212728 scopus 로고    scopus 로고
    • LAT is required for TCR-mediated activation of PLCγ1 and the Ras pathway
    • Finco, T.S., T. Kadlecek, W., Zhang, L.E. Samelson, and A. Weiss. 1998. LAT is required for TCR-mediated activation of PLCγ1 and the Ras pathway. Immunity. 9:617-626.
    • (1998) Immunity , vol.9 , pp. 617-626
    • Finco, T.S.1    Kadlecek, T.2    Zhang, W.3    Samelson, L.E.4    Weiss, A.5
  • 16
    • 0029100974 scopus 로고
    • Membrane transport in the endocytic pathway
    • Gruenberg, J., and F.R. Maxfield. 1995. Membrane transport in the endocytic pathway, Curr. Opin. Cell Biol. 7:552-563.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 552-563
    • Gruenberg, J.1    Maxfield, F.R.2
  • 17
    • 0034675889 scopus 로고    scopus 로고
    • Selective accumulation of raft-associated membrane protein LAT in T cell receptor signaling assemblies
    • Harder, T., and M. Kuhn. 2000. Selective accumulation of raft-associated membrane protein LAT in T cell receptor signaling assemblies. J. Cell Biol. 151:199-208.
    • (2000) J. Cell Biol. , vol.151 , pp. 199-208
    • Harder, T.1    Kuhn, M.2
  • 18
    • 0034069892 scopus 로고    scopus 로고
    • Interactions between Fc(epsilon)RI and lipid raft components are regulated by the actin cytoskeleton
    • Holowka, D., E.D. Sheets, and B. Baird. 2000. Interactions between Fc(epsilon)RI and lipid raft components are regulated by the actin cytoskeleton. J. Cell Sci. 113:1009-1019.
    • (2000) J. Cell Sci. , vol.113 , pp. 1009-1019
    • Holowka, D.1    Sheets, E.D.2    Baird, B.3
  • 19
    • 0020601856 scopus 로고
    • Internalization and processing of transferrin and the transferrin receptor in human carcinoma A431 cells
    • Hopkins, C.R., and I.S. Trowbridge. 1983. Internalization and processing of transferrin and the transferrin receptor in human carcinoma A431 cells. J Cell Biol. 97:508-521.
    • (1983) J. Cell Biol. , vol.97 , pp. 508-521
    • Hopkins, C.R.1    Trowbridge, I.S.2
  • 20
    • 0032727709 scopus 로고    scopus 로고
    • Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor
    • Janes, P.W., S.C. Ley, and A.I. Magee. 1999. Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor. Cell. Biol. 147:447-461.
    • (1999) Cell. Biol. , vol.147 , pp. 447-461
    • Janes, P.W.1    Ley, S.C.2    Magee, A.I.3
  • 21
    • 0034730188 scopus 로고    scopus 로고
    • A supramolecular basis for CD45 tyrosine phosphatase regulation in sustained T cell activation
    • Johnson, K.G., S.K. Bromley, M.L. Dustin, and M.L. Thomas. 2000. A supramolecular basis for CD45 tyrosine phosphatase regulation in sustained T cell activation. Proc. Natl. Acad. Sci. USA. 97:10138-10143.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10138-10143
    • Johnson, K.G.1    Bromley, S.K.2    Dustin, M.L.3    Thomas, M.L.4
  • 24
    • 0035147424 scopus 로고    scopus 로고
    • Multicolour imaging ofpost-Golgi sorting and trafficking in live cells
    • Keller, P., D. Toomre, E. Diaz, J. White, and K. Simons. 2001. Multicolour imaging ofpost-Golgi sorting and trafficking in live cells. Nat. Cell Biol. 3:140-149.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 140-149
    • Keller, P.1    Toomre, D.2    Diaz, E.3    White, J.4    Simons, K.5
  • 25
    • 0035525572 scopus 로고    scopus 로고
    • Positive and negative regulation of T-cell activation by adaptor proteins
    • Koretzky, G.A., and P.S. Myung. 2001. Positive and negative regulation of T-cell activation by adaptor proteins. Nat. Rev. Immunol. 1:95-107.
    • (2001) Nat. Rev. Immunol. , vol.1 , pp. 95-107
    • Koretzky, G.A.1    Myung, P.S.2
  • 26
    • 0034599541 scopus 로고    scopus 로고
    • Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton
    • Krause, M., A.S. Sechi, M. Konradt, D. Monner, F.B. Gertler, and J. Wehland. 2000. Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton. J. Cell Biol. 149:181-194.
    • (2000) J. Cell Biol. , vol.149 , pp. 181-194
    • Krause, M.1    Sechi, A.S.2    Konradt, M.3    Monner, D.4    Gertler, F.B.5    Wehland, J.6
  • 27
    • 0036467376 scopus 로고    scopus 로고
    • Dynamics of the immunological synapse: Finding, establishing and solidifying a connection
    • Krummel, M.F., and M.M. Davis. 2002. Dynamics of the immunological synapse: finding, establishing and solidifying a connection. Curr. Opin. Immunol. 14: 66-74.
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 66-74
    • Krummel, M.F.1    Davis, M.M.2
  • 28
    • 0034714184 scopus 로고    scopus 로고
    • Differential clustering of CD4 and CD3ζ during T cell recognition
    • Krummel, M.F., M.D. Sjaastad, C. Wulfing, and M.M. Davis. 2000. Differential clustering of CD4 and CD3ζ during T cell recognition. Science. 289:1349-1352.
    • (2000) Science , vol.289 , pp. 1349-1352
    • Krummel, M.F.1    Sjaastad, M.D.2    Wulfing, C.3    Davis, M.M.4
  • 29
    • 0037154747 scopus 로고    scopus 로고
    • T cell receptor signaling precedes immunological synapse formation
    • Lee, K.H., A.D. Holdorf, M.L. Dustin, A.C. Chan, P.M. Allen, and A.S. Shaw. 2002. T cell receptor signaling precedes immunological synapse formation. Science. 295:1539-1542.
    • (2002) Science , vol.295 , pp. 1539-1542
    • Lee, K.H.1    Holdorf, A.D.2    Dustin, M.L.3    Chan, A.C.4    Allen, P.M.5    Shaw, A.S.6
  • 30
    • 0032543221 scopus 로고    scopus 로고
    • T cell receptor-initiated calcium release is uncoupled from capacitative calcium entry in Irk-deficient T cells
    • Liu, K.Q., S.C. Bunnell, C.B. Gurniak, and L.J. Berg. 1998. T cell receptor-initiated calcium release is uncoupled from capacitative calcium entry in Irk-deficient T cells. J. Exp. Med. 187:1721-1727.
    • (1998) J. Exp. Med. , vol.187 , pp. 1721-1727
    • Liu, K.Q.1    Bunnell, S.C.2    Gurniak, C.B.3    Berg, L.J.4
  • 31
    • 0343181431 scopus 로고    scopus 로고
    • The hematopoietic-specific adaptor protein gads functions in T-cell signaling via interactions with the SLP-76 and LAT adaptors
    • Liu, S.K., N. Fang, G.A. Koretzky, and C.J. McGlade. 1999. The hematopoietic-specific adaptor protein gads functions in T-cell signaling via interactions with the SLP-76 and LAT adaptors. Curr. Biol. 9:67-75.
    • (1999) Curr. Biol. , vol.9 , pp. 67-75
    • Liu, S.K.1    Fang, N.2    Koretzky, G.A.3    McGlade, C.J.4
  • 32
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation clusters in T cells
    • Monks, C.R., B.A. Freiberg, H. Kupfet, N. Sciaky, and A. Kupfer. 1998. Three-dimensional segregation of supramolecular activation clusters in T cells. Nature. 395:82-86.
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.R.1    Freiberg, B.A.2    Kupfet, H.3    Sciaky, N.4    Kupfer, A.5
  • 33
    • 0029030937 scopus 로고
    • EEA1, an early endosome-associated protein. EEA1 is a conserved alpha-helical peripheral membrane protein flanked by cysteine "fingers" and contains a calmodulin-binding IQ motif
    • Mu, F.T., J.M. Callaghan, O. Steele-Mortimer, H. Stenmark, R.G. Parton, P.L. Campbell, J. McCluskey, J.P. Yeo, E.P. Tock, and B.H. Toh. 1995. EEA1, an early endosome-associated protein. EEA1 is a conserved alpha-helical peripheral membrane protein flanked by cysteine "fingers" and contains a calmodulin-binding IQ motif. Biol. Chem. 270:13503-13511.
    • (1995) Biol. Chem. , vol.270 , pp. 13503-13511
    • Mu, F.T.1    Callaghan, J.M.2    Steele-Mortimer, O.3    Stenmark, H.4    Parton, R.G.5    Campbell, P.L.6    McCluskey, J.7    Yeo, J.P.8    Tock, E.P.9    Toh, B.H.10
  • 34
    • 0030953187 scopus 로고    scopus 로고
    • The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner
    • Nakamura, N., M. Lowe, T.P. Levine, C. Rabouille, and G. Warren. 1997. The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner. Cell. 89:445-455.
    • (1997) Cell , vol.89 , pp. 445-455
    • Nakamura, N.1    Lowe, M.2    Levine, T.P.3    Rabouille, C.4    Warren, G.5
  • 36
    • 0030889062 scopus 로고    scopus 로고
    • Distinct compartmentalization of TGN46 and beta 1,4-galactosyltransferase in HeLa cells
    • Prescott, A.R., J.M. Lucocq, J. James, J.M. Lister, and S. Ponnambalam. 1997. Distinct compartmentalization of TGN46 and beta 1,4-galactosyltransferase in HeLa cells. Eur. J. Cell Biol. 72:238-246.
    • (1997) Eur. J. Cell Biol. , vol.72 , pp. 238-246
    • Prescott, A.R.1    Lucocq, J.M.2    James, J.3    Lister, J.M.4    Ponnambalam, S.5
  • 37
    • 0036225013 scopus 로고    scopus 로고
    • Imaging synapse formation during thymocyte selection: Inability of CD3ζ to form a stable central accumulation during negative selection
    • Richie, L.I., P.J. Ebert, L.C. Wu, M.F. Krummel, J.J. Owen, and M.M. Davis. 2002. Imaging synapse formation during thymocyte selection: inability of CD3ζ to form a stable central accumulation during negative selection. Immunity. 16:595-606.
    • (2002) Immunity , vol.16 , pp. 595-606
    • Richie, L.I.1    Ebert, P.J.2    Wu, L.C.3    Krummel, M.F.4    Owen, J.J.5    Davis, M.M.6
  • 38
    • 0036221481 scopus 로고    scopus 로고
    • Signal transduction mediated by the T cell antigen receptor: The role of adapter proteins
    • Samelson, L.E. 2002. Signal transduction mediated by the T cell antigen receptor: the role of adapter proteins. Annu. Rev. Immunol. 20:371-394.
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 371-394
    • Samelson, L.E.1
  • 39
    • 0030927323 scopus 로고    scopus 로고
    • Making the T cell receptor go the distance: A topological view of T cell activation
    • Shaw, A., and M.L. Dustin. 1997. Making the T cell receptor go the distance: a topological view of T cell activation. Immunity. 6:361-369.
    • (1997) Immunity , vol.6 , pp. 361-369
    • Shaw, A.1    Dustin, M.L.2
  • 40
    • 0032476650 scopus 로고    scopus 로고
    • ZAP-70 association with T cell receptor ζ (TCRζ): Fluorescence imaging of dynamic changes upon cellular stimulation
    • Sloan-Lancaster, J., J. Presley, J. Ellenberg, T. Yamazaki, J. Lippincott-Schwartz, and L.E. Samelson. 1998. ZAP-70 association with T cell receptor ζ (TCRζ): fluorescence imaging of dynamic changes upon cellular stimulation. J. Cell Biol. 143: 613-624.
    • (1998) J. Cell Biol. , vol.143 , pp. 613-624
    • Sloan-Lancaster, J.1    Presley, J.2    Ellenberg, J.3    Yamazaki, T.4    Lippincott-Schwartz, J.5    Samelson, L.E.6
  • 41
    • 0032534304 scopus 로고    scopus 로고
    • TCR signaling induces selective exclusion of CD43 from the T cell-antigen-presenting cell contact site
    • Sperling, A.I., J.R. Sedy, N. Manjunath, A. Kupfer, B. Ardman, and J.K. Burkhardt. 1998. TCR signaling induces selective exclusion of CD43 from the T cell-antigen-presenting cell contact site. J. Immunol 161:6459-6462.
    • (1998) J. Immunol. , vol.161 , pp. 6459-6462
    • Sperling, A.I.1    Sedy, J.R.2    Manjunath, N.3    Kupfer, A.4    Ardman, B.5    Burkhardt, J.K.6
  • 42
    • 0033054154 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system and endocytosis
    • Strous, G.J., and R. Govers. 1999. The ubiquitin-proteasome system and endocytosis. J. Cell Sci. 112:1417-1423.
    • (1999) J. Cell Sci. , vol.112 , pp. 1417-1423
    • Strous, G.J.1    Govers, R.2
  • 43
    • 0029850677 scopus 로고    scopus 로고
    • Rab11 regulates recycling through the pericentriolar recycling endosome
    • Ullrich, O., S. Reinsch, S. Urbe, M. Zerial, and R.G. Parton. 1996. Rab11 regulates recycling through the pericentriolar recycling endosome. J. Cell Biol. 135:913-924.
    • (1996) J. Cell Biol. , vol.135 , pp. 913-924
    • Ullrich, O.1    Reinsch, S.2    Urbe, S.3    Zerial, M.4    Parton, R.G.5
  • 44
    • 0035817631 scopus 로고    scopus 로고
    • High resolution mapping of mast cell membranes reveals primary and secondary domains of FcεRI and LAT
    • Wilson, B.S., J.R. Pfeiffer, Z. Surviladze, E.A. Gaudet, and J.M. Oliver. 2001. High resolution mapping of mast cell membranes reveals primary and secondary domains of FcεRI and LAT. Cell Biol. 154:645-658.
    • (2001) Cell Biol. , vol.154 , pp. 645-658
    • Wilson, B.S.1    Pfeiffer, J.R.2    Surviladze, Z.3    Gaudet, E.A.4    Oliver, J.M.5
  • 45
    • 0001584956 scopus 로고    scopus 로고
    • Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation
    • Wu, J., D.G. Motto, G.A. Koetzky, and A. Weiss. 1996. Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation. Immunity. 4:593-602.
    • (1996) Immunity , vol.4 , pp. 593-602
    • Wu, J.1    Motto, D.G.2    Koetzky, G.A.3    Weiss, A.4
  • 46
    • 0032545218 scopus 로고    scopus 로고
    • A receptor/cytoskeletal movement triggered by costimulation during T cell activation
    • Wulfing, C., and M.M. Davis. 1998. A receptor/cytoskeletal movement triggered by costimulation during T cell activation. Science. 282:2266-2269.
    • (1998) Science , vol.282 , pp. 2266-2269
    • Wulfing, C.1    Davis, M.M.2
  • 47
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T cell activation
    • Xavier, R., T. Brennan, Q. Li, C. McCormack, and B. Seed. 1998. Membrane compartmentation is required for efficient T cell activation. Immunity. 8:723-732.
    • (1998) Immunity , vol.8 , pp. 723-732
    • Xavier, R.1    Brennan, T.2    Li, Q.3    McCormack, C.4    Seed, B.5
  • 48
    • 0034768532 scopus 로고    scopus 로고
    • Mechanisms of signaling by the hematopoietic-specific adaptor proteins, SLP-76 and LAT and their B cell counterpart, BLNK/SLP-65
    • Yablonski, D., and A. Weiss. 2001. Mechanisms of signaling by the hematopoietic-specific adaptor proteins, SLP-76 and LAT and their B cell counterpart, BLNK/SLP-65. Adv. Immunol. 79:93-128.
    • (2001) Adv. Immunol. , vol.79 , pp. 93-128
    • Yablonski, D.1    Weiss, A.2
  • 49
    • 0032541062 scopus 로고    scopus 로고
    • Uncoupling of nonreceptor tyrosine kinases from PLC-gamma1 in an SLP-76-deficient T cell
    • Yablonski, D., M.R. Kuhne, T. Kadlecek, and A. Weiss. 1998. Uncoupling of nonreceptor tyrosine kinases from PLC-gamma1 in an SLP-76-deficient T cell. Science. 281:413-416.
    • (1998) Science , vol.281 , pp. 413-416
    • Yablonski, D.1    Kuhne, M.R.2    Kadlecek, T.3    Weiss, A.4
  • 50
    • 0034972991 scopus 로고    scopus 로고
    • Identification of a phospholipase C-γ1 (PLC-γ1) SH3 domain-binding site in SLP-76 required for T-cell receptor-mediated activation of PLC-γ1 and NFAT
    • Yablonski, D., T. Kadlecek, and A. Weiss. 2001. Identification of a phospholipase C-γ1 (PLC-γ1) SH3 domain-binding site in SLP-76 required for T-cell receptor-mediated activation of PLC-γ1 and NFAT. Mol. Cell. Biol. 21: 4208-4218.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4208-4218
    • Yablonski, D.1    Kadlecek, T.2    Weiss, A.3
  • 52
    • 0036224370 scopus 로고    scopus 로고
    • Inhibition of T cell receptor-coreceptor interactions by antagonist ligands visualized by live FRET imaging of the T-hybridoma immunological synapse
    • Zal, T., M.A. Zal, and N.R. Gascoigne. 2002. Inhibition of T cell receptor-coreceptor interactions by antagonist ligands visualized by live FRET imaging of the T-hybridoma immunological synapse. Immunity. 16:521-534.
    • (2002) Immunity , vol.16 , pp. 521-534
    • Zal, T.1    Zal, M.A.2    Gascoigne, N.R.3
  • 53
    • 0032992072 scopus 로고    scopus 로고
    • Functional analysis of LAT in TCR-mediated signaling pathways using a LAT-deficient Jurkat cell line
    • Zhang, W., B.J. Irvin, R.P. Trible, R.T. Abraham, and L.E. Samelson. 1999. Functional analysis of LAT in TCR-mediated signaling pathways using a LAT-deficient Jurkat cell line. Int. Immunol. 11:943-950.
    • (1999) Int. Immunol. , vol.11 , pp. 943-950
    • Zhang, W.1    Irvin, B.J.2    Trible, R.P.3    Abraham, R.T.4    Samelson, L.E.5
  • 54
    • 0032498231 scopus 로고    scopus 로고
    • LAT: The ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation
    • Zhang, W., J. Sloan-Lancaster, J. Kitchen, R.P. Trible, and L.E. Samelson. 1998a. LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell. 92:83-92.
    • (1998) Cell , vol.92 , pp. 83-92
    • Zhang, W.1    Sloan-Lancaster, J.2    Kitchen, J.3    Trible, R.P.4    Samelson, L.E.5
  • 55
    • 0032142953 scopus 로고    scopus 로고
    • LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation
    • Zhang, W., R.P. Trible, and L.E. Samelson. 1998b. LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. Immunity. 9:239-246.
    • (1998) Immunity , vol.9 , pp. 239-246
    • Zhang, W.1    Trible, R.P.2    Samelson, L.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.